Enzymes can provide extraordinary protection against toxic compounds. The enzymatic detoxification of malathion is one example. Malalhion is a very effective insecticide when used against fruit flies, yet it has very little toxic effect on humans due to its detoxification in the liver by the enzyme carboxylesterase. The species and target selectivity provided by enzymes allows for uses in a variety of complex backgrounds with little to no risk of harm to desirable organisms or components in the background.
VX ((Ethyl {2-[bis(propan-2-yl)amino]ethyl}sulfanyl) (methyl)phosphinate is one of the most toxic compounds known in humans. The median lethal dose (LD50) for humans is estimated to be about 10 milligrams when contact is through skin. The estimated LCt50 for inhalation is estimated to be 30-50 mg·min/m3. No efficient and easily produced catalyst for VX degradation in the environment or in vivo is known. One enzyme, phosphotriesterase (PTE), also known as organophosphorus hydrolase (OPH), has previously been reported to possess VX activity. However, PTE is not easily produced in bacteria at high concentrations necessitating more complex synthesis procedures and increasing the difficulty of obtaining sufficient, active quantities of the enzyme to be useful in an environmental setting.
As such, new compounds and methods for the specific degradation of VX are needed.